Faculty Opinions recommendation of Clarinet (CLA-1), a novel active zone protein required for synaptic vesicle clustering and release.

Author(s):  
Jens Rettig ◽  
David Stevens
Keyword(s):  
2014 ◽  
Vol 11 (10) ◽  
pp. 971-980 ◽  
Author(s):  
Melanie Laßek ◽  
Jens Weingarten ◽  
Amparo Acker-Palmer ◽  
Sandra Bajjalieh ◽  
Ulrike Muller ◽  
...  

2021 ◽  
Vol 559 ◽  
pp. 92-98
Author(s):  
Judyta K. Juranek ◽  
Konark Mukherjee ◽  
Reinhard Jahn ◽  
Jia-Yi Li

2011 ◽  
Vol 108 (25) ◽  
pp. E222-E229 ◽  
Author(s):  
F. Kawasaki ◽  
J. Iyer ◽  
L. L. Posey ◽  
C. E. Sun ◽  
S. E. Mammen ◽  
...  

2008 ◽  
Vol 25 (4) ◽  
pp. 523-533 ◽  
Author(s):  
QUN-FANG WAN ◽  
ALEJANDRO VILA ◽  
ZHEN-YU ZHOU ◽  
RUTH HEIDELBERGER

AbstractTo better understand synaptic signaling at the mammalian rod bipolar cell terminal and pave the way for applying genetic approaches to the study of visual information processing in the mammalian retina, synaptic vesicle dynamics and intraterminal calcium were monitored in terminals of acutely isolated mouse rod bipolar cells and the number of ribbon-style active zones quantified. We identified a releasable pool, corresponding to a maximum of ≈35 vesicles/ribbon-style active zone. Following depletion, this pool was refilled with a time constant of ≈7 s. The presence of a smaller, rapidly releasing pool and a small, fast component of refilling was also suggested. Following calcium channel closure, membrane surface area was restored to baseline with a time constant that ranged from 2 to 21 s depending on the magnitude of the preceding Ca2+ transient. In addition, a brief, calcium-dependent delay often preceded the start of onset of membrane recovery. Thus, several aspects of synaptic vesicle dynamics appear to be conserved between rod-dominant bipolar cells of fish and mammalian rod bipolar cells. A major difference is that the number of vesicles available for release is significantly smaller in the mouse rod bipolar cell, both as a function of the total number per neuron and on a per active zone basis.


Author(s):  
Peggy Mason

The biochemical and physiological processes of neurotransmitter release from an active zone, a specialized region of synaptic membrane, are examined. Synaptic vesicles containing neurotransmitters are docked at the active zone and then primed for release by SNARE complexes that bring them into extreme proximity to the plasma membrane. Entry of calcium ions through voltage-gated calcium channels triggers synaptic vesicle fusion with the synaptic terminal membrane and the consequent diffusion of neurotransmitter into the synaptic cleft. Release results when the fusion pore bridging the synaptic vesicle and plasma membrane widens and neurotransmitter from the inside of the synaptic vesicle diffuses into the synaptic cleft. Membrane from the active zone membrane is endocytosed, and synaptic vesicle proteins are then reassembled into recycled synaptic vesicles, allowing for more rounds of neurotransmitter release.


PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e26164 ◽  
Author(s):  
Laura Torres-Benito ◽  
Margret Feodora Neher ◽  
Raquel Cano ◽  
Rocio Ruiz ◽  
Lucia Tabares

PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e69410 ◽  
Author(s):  
Mark L. Harlow ◽  
Joseph A. Szule ◽  
Jing Xu ◽  
Jae Hoon Jung ◽  
Robert M. Marshall ◽  
...  

2020 ◽  
Author(s):  
Zhuo Guan ◽  
Mónica C. Quiñones-Frías ◽  
Yulia Akbergenova ◽  
J. Troy Littleton

AbstractSynchronous neurotransmitter release is triggered by Ca2+ binding to the synaptic vesicle protein Synaptotagmin 1, while asynchronous fusion and short-term facilitation is hypothesized to be mediated by plasma membrane-localized Synaptotagmin 7 (SYT7). We generated mutations in Drosophila Syt7 to determine if it plays a conserved role as the Ca2+ sensor for these processes. Electrophysiology and quantal imaging revealed evoked release was elevated 2-fold. Syt7 mutants also had a larger pool of readily-releasable vesicles, faster recovery following stimulation, and robust facilitation. Syt1/Syt7 double mutants displayed more release than Syt1 mutants alone, indicating SYT7 does not mediate the residual asynchronous release remaining in the absence of SYT1. SYT7 localizes to an internal membrane tubular network within the peri-active zone, but does not enrich at release sites. These findings indicate the two Ca2+ sensor model of SYT1 and SYT7 mediating all phases of neurotransmitter release and facilitation is not applicable at Drosophila synapses.


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